The glycoprotein chlorperoxidase (CPO) from the marine fungus Caldariomyces fumago is the most versatile of all the heme enzymes known. In addition to its biological function of catalyzing peroxide dependent halogenation reactions, this enzyme can catalyze the reactions of catalase, peroxidase and cytochrome P450. It catalyzes enantioselective oxidation of a wide range of organic substrates, which makes it a potential industrial enzyme. Structurally, this protein has a unique fold and a large number of ordered carbohydrates. We have reported the crystal structure of CPO at 1.9 E resolution. Earlier tests indicated that the CPO crystals can diffract to better 1.4 E resolution under cryogenic conditions in synchrotron X-radiation. CPO structure determined at higher resolution is expected to show more ordered carbohydrate structure and increase our understanding of the structure glycoproteins.